Maruyama K, Kimura M, Kimura S, Ohashi K, Suzuki K, Katunuma N
J Biochem. 1981 Mar;89(3):711-5. doi: 10.1093/oxfordjournals.jbchem.a133250.
The effects of various proteolytic enzymes on the high molecular weight protein (connectin) present in a direct sodium dodecyl sulfate extract of myofibrils from chicken breast muscle were studied in detail. To keep the high molecular weight proteins intact, myofibrils had to be prepared in the presence of EGTA. Trypsin, chymotrypsin, papain, and nagarse readily hydrolyzed connectin (doublet band of titin) and the band 3 protein (N2-line protein). Pepsin did not attack connectin, but digested the band 3 protein and myosin. Calcium-activated neutral proteinase hydrolyzed the band 3 protein, leaving connectin intact. On the other hand, serine protease digested connectin but not the band 3 protein.
详细研究了各种蛋白水解酶对鸡胸肌肌原纤维的十二烷基硫酸钠直接提取物中存在的高分子量蛋白质(连接蛋白)的影响。为了保持高分子量蛋白质的完整性,必须在乙二醇双(2-氨基乙基醚)四乙酸(EGTA)存在的情况下制备肌原纤维。胰蛋白酶、胰凝乳蛋白酶、木瓜蛋白酶和纳加酶很容易水解连接蛋白(肌联蛋白的双峰带)和带3蛋白(N2线蛋白)。胃蛋白酶不攻击连接蛋白,但能消化带3蛋白和肌球蛋白。钙激活中性蛋白酶水解带3蛋白,使连接蛋白保持完整。另一方面,丝氨酸蛋白酶消化连接蛋白,但不消化带3蛋白。